{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T12:45:08Z","timestamp":1792759508884,"version":"4.5.0"},"reference-count":151,"publisher":"Elsevier BV","license":[{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T00:00:00Z","timestamp":1790812800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2026,8,29]],"date-time":"2026-08-29T00:00:00Z","timestamp":1787961600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/100000135","name":"National Institutes of Health Blueprint for Neuroscience Research","doi-asserted-by":"publisher","award":["RO1 DK125897"],"award-info":[{"award-number":["RO1 DK125897"]}],"id":[{"id":"10.13039\/100000135","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100002426","name":"Telethon Foundation","doi-asserted-by":"publisher","award":["TS001324"],"award-info":[{"award-number":["TS001324"]}],"id":[{"id":"10.13039\/501100002426","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100005010","name":"Associazione Italiana per la Ricerca sul Cancro","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100005010","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/100020581","name":"AIRC Foundation for Cancer Research","doi-asserted-by":"publisher","award":["IG 28733"],"award-info":[{"award-number":["IG 28733"]}],"id":[{"id":"10.13039\/100020581","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Pharmacological Research"],"published-print":{"date-parts":[[2026,10]]},"DOI":"10.1016\/j.phrs.2026.108428","type":"journal-article","created":{"date-parts":[[2026,9,1]],"date-time":"2026-09-01T00:20:51Z","timestamp":1788222051000},"page":"108428","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":3,"special_numbering":"C","title":["Crosstalk between UPR and mitochondria: The triad of ER\u2013mitochondria contacts, Ca\u00b2\u207a, and ROS"],"prefix":"10.1016","volume":"232","author":[{"ORCID":"https:\/\/orcid.org\/0000-0001-7786-7698","authenticated-orcid":false,"given":"Ester","family":"Zito","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Gy\u00f6rgy","family":"Hajn\u00f3czky","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.phrs.2026.108428_bib1","doi-asserted-by":"crossref","first-page":"1081","DOI":"10.1126\/science.1209038","article-title":"The unfolded protein response: from stress pathway to homeostatic regulation","volume":"334","author":"Walter","year":"2011","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib2","doi-asserted-by":"crossref","first-page":"1374","DOI":"10.15252\/embr.201642195","article-title":"The integrated stress response","volume":"17","author":"Pakos-Zebrucka","year":"2016","journal-title":"EMBO Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib3","doi-asserted-by":"crossref","first-page":"3066","DOI":"10.1101\/gad.1250704","article-title":"CHOP induces death by promoting protein synthesis and oxidation in the stressed endoplasmic reticulum","author":"Marciniak","year":"2004","journal-title":"Genes. Dev. 18"},{"key":"10.1016\/j.phrs.2026.108428_bib4","doi-asserted-by":"crossref","first-page":"523","DOI":"10.1016\/j.tcb.2018.02.009","article-title":"Endoplasmic reticulum-mitochondrial contactology: structure and signaling functions","volume":"28","author":"Csordas","year":"2018","journal-title":"Trends Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib5","doi-asserted-by":"crossref","first-page":"2143","DOI":"10.1242\/jcs.080762","article-title":"Increased ER-mitochondrial coupling promotes mitochondrial respiration and bioenergetics during early phases of ER stress","volume":"124","author":"Bravo","year":"2011","journal-title":"J. Cell. Sci."},{"key":"10.1016\/j.phrs.2026.108428_bib6","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2022.111899","article-title":"The endoplasmic reticulum kinase PERK interacts with the oxidoreductase ERO1 to metabolically adapt mitochondria","volume":"42","author":"Bassot","year":"2023","journal-title":"Cell. Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib7","doi-asserted-by":"crossref","first-page":"755","DOI":"10.1038\/s41556-019-0329-y","article-title":"Non-canonical function of IRE1alpha determines mitochondria-associated endoplasmic reticulum composition to control calcium transfer and bioenergetics","volume":"21","author":"Carreras-Sureda","year":"2019","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib8","first-page":"29","article-title":"ER stress and the unfolded protein response","volume":"569","author":"Schroder","year":"2005","journal-title":"Mutat. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib9","doi-asserted-by":"crossref","first-page":"562","DOI":"10.1016\/j.cell.2009.07.017","article-title":"IRE1alpha kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates","volume":"138","author":"Han","year":"2009","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib10","doi-asserted-by":"crossref","first-page":"245","DOI":"10.1016\/j.tibs.2014.02.008","article-title":"Getting RIDD of RNA: IRE1 in cell fate regulation","volume":"39","author":"Maurel","year":"2014","journal-title":"Trends Biochem. Sci."},{"key":"10.1016\/j.phrs.2026.108428_bib11","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1016\/S1097-2765(00)00133-7","article-title":"ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs","volume":"6","author":"Ye","year":"2000","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib12","doi-asserted-by":"crossref","first-page":"3787","DOI":"10.1091\/mbc.10.11.3787","article-title":"Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress","volume":"10","author":"Haze","year":"1999","journal-title":"Mol. Biol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib13","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/16729","article-title":"Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase","volume":"397","author":"Harding","year":"1999","journal-title":"Nature"},{"key":"10.1016\/j.phrs.2026.108428_bib14","doi-asserted-by":"crossref","first-page":"7198","DOI":"10.1128\/MCB.23.20.7198-7209.2003","article-title":"Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival","volume":"23","author":"Cullinan","year":"2003","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib15","doi-asserted-by":"crossref","DOI":"10.1038\/srep32886","article-title":"Integrated stress response of vertebrates is regulated by four eIF2alpha kinases","volume":"6","author":"Taniuchi","year":"2016","journal-title":"Sci. Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib16","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1016\/S1097-2765(03)00105-9","article-title":"An integrated stress response regulates amino acid metabolism and resistance to oxidative stress","volume":"11","author":"Harding","year":"2003","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib17","doi-asserted-by":"crossref","first-page":"638","DOI":"10.1038\/cdd.2016.158","article-title":"dATF4 regulation of mitochondrial folate-mediated one-carbon metabolism is neuroprotective","volume":"24","author":"Celardo","year":"2017","journal-title":"Cell. Death Differ."},{"key":"10.1016\/j.phrs.2026.108428_bib18","doi-asserted-by":"crossref","DOI":"10.1126\/science.aat5314","article-title":"The integrated stress response: From mechanism to disease","volume":"368","author":"Costa-Mattioli","year":"2020","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib19","doi-asserted-by":"crossref","first-page":"1880","DOI":"10.1038\/cdd.2012.74","article-title":"PERK is required at the ER-mitochondrial contact sites to convey apoptosis after ROS-based ER stress","volume":"19","author":"Verfaillie","year":"2012","journal-title":"Cell. Death Differ."},{"key":"10.1016\/j.phrs.2026.108428_bib20","doi-asserted-by":"crossref","first-page":"2348","DOI":"10.1038\/emboj.2013.168","article-title":"Mfn2 modulates the UPR and mitochondrial function via repression of PERK","volume":"32","author":"Munoz","year":"2013","journal-title":"EMBO J."},{"key":"10.1016\/j.phrs.2026.108428_bib21","doi-asserted-by":"crossref","DOI":"10.1126\/sciadv.abf0971","article-title":"Adaptation to mitochondrial stress requires CHOP-directed tuning of ISR","volume":"7","author":"Kaspar","year":"2021","journal-title":"Sci. Adv."},{"key":"10.1016\/j.phrs.2026.108428_bib22","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1016\/S1097-2765(00)80017-9","article-title":"The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum","volume":"1","author":"Frand","year":"1998","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib23","doi-asserted-by":"crossref","first-page":"171","DOI":"10.1016\/S1097-2765(00)80018-0","article-title":"Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum","volume":"1","author":"Pollard","year":"1998","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib24","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1016\/S1097-2765(02)00696-2","article-title":"The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum","volume":"10","author":"Tu","year":"2002","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib25","doi-asserted-by":"crossref","first-page":"787","DOI":"10.1016\/j.molcel.2010.11.010","article-title":"Oxidative protein folding by an endoplasmic reticulum-localized peroxiredoxin","volume":"40","author":"Zito","year":"2010","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib26","doi-asserted-by":"crossref","first-page":"39","DOI":"10.1016\/j.molcel.2012.08.010","article-title":"Endoplasmic Reticulum Thiol Oxidase Deficiency Leads to Ascorbic Acid Depletion and Noncanonical Scurvy in Mice","volume":"48","author":"Zito","year":"2012","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib27","doi-asserted-by":"crossref","first-page":"14","DOI":"10.1016\/j.redox.2015.11.004","article-title":"Cysteines 208 and 241 in Ero1alpha are required for maximal catalytic turnover","volume":"7","author":"Ramming","year":"2016","journal-title":"Redox Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib28","doi-asserted-by":"crossref","first-page":"39513","DOI":"10.1074\/jbc.M112.405050","article-title":"Hyperactivity of the Ero1alpha oxidase elicits endoplasmic reticulum stress but no broad antioxidant response","volume":"287","author":"Hansen","year":"2012","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib29","doi-asserted-by":"crossref","first-page":"1077","DOI":"10.1089\/ars.2011.4004","article-title":"Ero1alpha regulates Ca(2+) fluxes at the endoplasmic reticulum-mitochondria interface (MAM)","volume":"16","author":"Anelli","year":"2012","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.phrs.2026.108428_bib30","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1161\/CIRCRESAHA.121.320531","article-title":"Ero1alpha-Dependent ERp44 Dissociation From RyR2 Contributes to Cardiac Arrhythmia","volume":"130","author":"Hamilton","year":"2022","journal-title":"Circ. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib31","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/j.cell.2004.11.048","article-title":"Subtype-specific and ER lumenal environment-dependent regulation of inositol 1,4,5-trisphosphate receptor type 1 by ERp44","volume":"120","author":"Higo","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib32","doi-asserted-by":"crossref","first-page":"783","DOI":"10.1083\/jcb.200904060","article-title":"Role of ERO1-alpha-mediated stimulation of inositol 1,4,5-triphosphate receptor activity in endoplasmic reticulum stress-induced apoptosis","volume":"186","author":"Li","year":"2009","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib33","doi-asserted-by":"crossref","first-page":"767","DOI":"10.1016\/j.molcel.2004.08.025","article-title":"Degradation of misfolded proteins prevents ER-derived oxidative stress and cell death","volume":"15","author":"Haynes","year":"2004","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib34","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1038\/sj.onc.1210638","article-title":"Endoplasmic reticulum stress induces calcium-dependent permeability transition, mitochondrial outer membrane permeabilization and apoptosis","volume":"27","author":"Deniaud","year":"2008","journal-title":"Oncogene"},{"key":"10.1016\/j.phrs.2026.108428_bib35","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1016\/j.freeradbiomed.2012.06.042","article-title":"Deficiency of alphaB crystallin augments ER stress-induced apoptosis by enhancing mitochondrial dysfunction","volume":"53","author":"Dou","year":"2012","journal-title":"Free. Radic. Biol. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib36","doi-asserted-by":"crossref","first-page":"84","DOI":"10.1002\/hep.30507","article-title":"Deficiency of Mitochondrial Glycerol 3-Phosphate Dehydrogenase Contributes to Hepatic Steatosis","volume":"70","author":"Zheng","year":"2019","journal-title":"Hepatology"},{"key":"10.1016\/j.phrs.2026.108428_bib37","article-title":"Melatonin Can Modulate the Effect of Navitoclax (ABT-737) in HL-60 Cells","volume":"9","author":"Lomovsky","year":"2020","journal-title":"Antioxid. (Basel)"},{"key":"10.1016\/j.phrs.2026.108428_bib38","doi-asserted-by":"crossref","first-page":"7248","DOI":"10.1016\/S0021-9258(19)39106-9","article-title":"Phospholipid synthesis in a membrane fraction associated with mitochondria","volume":"265","author":"Vance","year":"1990","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib39","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1002\/biof.5520080309","article-title":"Electron microscopic tomography of rat-liver mitochondria and their interaction with the endoplasmic reticulum","volume":"8","author":"Mannella","year":"1998","journal-title":"Biofactors"},{"key":"10.1016\/j.phrs.2026.108428_bib40","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1083\/jcb.200604016","article-title":"Structural and functional features and significance of the physical linkage between ER and mitochondria","volume":"174","author":"Csordas","year":"2006","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib41","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/j.molcel.2010.06.029","article-title":"Imaging interorganelle contacts and local calcium dynamics at the ER-mitochondrial interface","volume":"39","author":"Csordas","year":"2010","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib42","doi-asserted-by":"crossref","first-page":"1417","DOI":"10.1038\/cdd.2016.52","article-title":"The coming of age of the mitochondria-ER contact: a matter of thickness","volume":"23","author":"Giacomello","year":"2016","journal-title":"Cell. Death Differ."},{"key":"10.1016\/j.phrs.2026.108428_bib43","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1083\/jcb.200608073","article-title":"Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca2+ channels","volume":"175","author":"Szabadkai","year":"2006","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib44","doi-asserted-by":"crossref","first-page":"456","DOI":"10.1038\/s41580-024-00820-1","article-title":"The roles of mitochondria in global and local intracellular calcium signalling","volume":"26","author":"Cartes-Saavedra","year":"2025","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib45","doi-asserted-by":"crossref","first-page":"605","DOI":"10.1038\/nature07534","article-title":"Mitofusin 2 tethers endoplasmic reticulum to mitochondria","volume":"456","author":"de Brito","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.phrs.2026.108428_bib46","doi-asserted-by":"crossref","first-page":"1165","DOI":"10.1016\/j.cell.2008.12.005","article-title":"Mitofusin 2 builds a bridge between ER and mitochondria","volume":"135","author":"Merkwirth","year":"2008","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib47","doi-asserted-by":"crossref","first-page":"1299","DOI":"10.1093\/hmg\/ddr559","article-title":"VAPB interacts with the mitochondrial protein PTPIP51 to regulate calcium homeostasis","volume":"21","author":"De Vos","year":"2012","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.phrs.2026.108428_bib48","doi-asserted-by":"crossref","first-page":"3401","DOI":"10.1038\/s41467-025-58538-3","article-title":"Mitochondrial complexity is regulated at ER-mitochondria contact sites via PDZD8-FKBP8 tethering","volume":"16","author":"Nakamura","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib49","doi-asserted-by":"crossref","first-page":"717","DOI":"10.1038\/sj.emboj.7600559","article-title":"PACS-2 controls endoplasmic reticulum-mitochondria communication and Bid-mediated apoptosis","volume":"24","author":"Simmen","year":"2005","journal-title":"EMBO J."},{"key":"10.1016\/j.phrs.2026.108428_bib50","doi-asserted-by":"crossref","first-page":"623","DOI":"10.1126\/science.aan6009","article-title":"ER-mitochondria tethering by PDZD8 regulates Ca(2+) dynamics in mammalian neurons","volume":"358","author":"Hirabayashi","year":"2017","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib51","doi-asserted-by":"crossref","first-page":"595","DOI":"10.1016\/j.bbalip.2013.11.014","article-title":"MAM (mitochondria-associated membranes) in mammalian cells: lipids and beyond","volume":"1841","author":"Vance","year":"2014","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.phrs.2026.108428_bib52","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1126\/science.1178016","article-title":"Cell biology. Connecting organelles","volume":"325","author":"Wiedemann","year":"2009","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib53","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1016\/j.molcel.2016.05.040","article-title":"Redox Nanodomains Are Induced by and Control Calcium Signaling at the ER-Mitochondrial Interface","volume":"63","author":"Booth","year":"2016","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib54","doi-asserted-by":"crossref","first-page":"1352","DOI":"10.1016\/j.bbabio.2009.06.004","article-title":"SR\/ER-mitochondrial local communication: calcium and ROS","volume":"1787","author":"Csordas","year":"2009","journal-title":"Biochim. Biophys. Acta"},{"key":"10.1016\/j.phrs.2026.108428_bib55","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/j.cell.2023.11.040","article-title":"Making the connection: How membrane contact sites have changed our view of organelle biology","volume":"187","author":"Voeltz","year":"2024","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib56","doi-asserted-by":"crossref","first-page":"902","DOI":"10.1038\/s41556-025-01668-z","article-title":"Endoplasmic reticulum-mitochondria contacts are prime hotspots of phospholipid peroxidation driving ferroptosis","volume":"27","author":"Sassano","year":"2025","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib57","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1042\/BST20150272","article-title":"When under pressure, get closer: PERKing up membrane contact sites during ER stress","volume":"44","author":"van Vliet","year":"2016","journal-title":"Biochem. Soc. Trans."},{"key":"10.1016\/j.phrs.2026.108428_bib58","doi-asserted-by":"crossref","DOI":"10.1242\/jcs.218479","article-title":"Mechanical forces on cellular organelles","volume":"131","author":"Feng","year":"2018","journal-title":"J. Cell. Sci."},{"key":"10.1016\/j.phrs.2026.108428_bib59","doi-asserted-by":"crossref","first-page":"525","DOI":"10.1083\/jcb.200907074","article-title":"Membrane expansion alleviates endoplasmic reticulum stress independently of the unfolded protein response","volume":"187","author":"Schuck","year":"2009","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib60","doi-asserted-by":"crossref","DOI":"10.1016\/j.ceca.2023.102719","article-title":"The mitochondrial permeability transition pore in Ca(2+) homeostasis","volume":"111","author":"Carraro","year":"2023","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib61","doi-asserted-by":"crossref","first-page":"20796","DOI":"10.1074\/jbc.M109.025353","article-title":"Calcium elevation in mitochondria is the main Ca2+ requirement for mitochondrial permeability transition pore (mPTP) opening","volume":"284","author":"Baumgartner","year":"2009","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib62","doi-asserted-by":"crossref","DOI":"10.1083\/jcb.202206008","article-title":"PERK recruits E-Syt1 at ER-mitochondria contacts for mitochondrial lipid transport and respiration","volume":"222","author":"Sassano","year":"2023","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib63","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0076941","article-title":"Sigma-1 receptor chaperone at the ER-mitochondrion interface mediates the mitochondrion-ER-nucleus signaling for cellular survival","volume":"8","author":"Mori","year":"2013","journal-title":"PLoS. One"},{"key":"10.1016\/j.phrs.2026.108428_bib64","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/j.freeradbiomed.2015.01.011","article-title":"ERO1: A protein disulfide oxidase and H2O2 producer","volume":"83","author":"Zito","year":"2015","journal-title":"Free. Radic. Biol. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib65","doi-asserted-by":"crossref","DOI":"10.1038\/s41556-026-01980-2","article-title":"ERO1a fosters glioblastoma aggressiveness and metabolic flexibility by regulating mitochondria-associated membrane dynamics","author":"Bassot","year":"2026","journal-title":"Nat. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib66","doi-asserted-by":"crossref","first-page":"3229","DOI":"10.1021\/bi00177a013","article-title":"Human, mouse, and rat calnexin cDNA cloning: identification of potential calcium binding motifs and gene localization to human chromosome 5","volume":"33","author":"Tjoelker","year":"1994","journal-title":"Biochemistry"},{"key":"10.1016\/j.phrs.2026.108428_bib67","doi-asserted-by":"crossref","DOI":"10.7554\/eLife.62601","article-title":"Calcium depletion challenges endoplasmic reticulum proteostasis by destabilising BiP-substrate complexes","volume":"9","author":"Preissler","year":"2020","journal-title":"Elife"},{"key":"10.1016\/j.phrs.2026.108428_bib68","doi-asserted-by":"crossref","first-page":"30873","DOI":"10.1074\/jbc.272.49.30873","article-title":"BiP, a major chaperone protein of the endoplasmic reticulum lumen, plays a direct and important role in the storage of the rapidly exchanging pool of Ca2+","volume":"272","author":"Lievremont","year":"1997","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib69","doi-asserted-by":"crossref","first-page":"291","DOI":"10.1016\/j.ceca.2005.06.033","article-title":"Modulating sarco(endo)plasmic reticulum Ca2+ ATPase 2 (SERCA2) activity: cell biological implications","volume":"38","author":"Vangheluwe","year":"2005","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib70","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1016\/j.semcdb.2019.01.012","article-title":"Spatial-temporal patterning of Ca(2+) signals by the subcellular distribution of IP(3) and IP(3) receptors","volume":"94","author":"Lock","year":"2019","journal-title":"Semin. Cell. Dev. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib71","doi-asserted-by":"crossref","first-page":"3726","DOI":"10.1038\/s41467-019-11646-3","article-title":"IP(3) receptor isoforms differently regulate ER-mitochondrial contacts and local calcium transfer","volume":"10","author":"Bartok","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib72","article-title":"The evolution of the mitochondria-to-calcium release units relationship in vertebrate skeletal muscles","volume":"2011","author":"Franzini-Armstrong","year":"2011","journal-title":"J. Biomed. Biotechnol."},{"key":"10.1016\/j.phrs.2026.108428_bib73","first-page":"261","article-title":"ER-mitochondria communication. How privileged?","volume":"22","author":"Franzini-Armstrong","year":"2007","journal-title":"Physiol. (Bethesda)"},{"key":"10.1016\/j.phrs.2026.108428_bib74","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1146\/annurev-biochem-060614-034216","article-title":"Enjoy the Trip: Calcium in Mitochondria Back and Forth","volume":"85","author":"De Stefani","year":"2016","journal-title":"Annu. Rev. Biochem."},{"key":"10.1016\/j.phrs.2026.108428_bib75","doi-asserted-by":"crossref","first-page":"1763","DOI":"10.1126\/science.280.5370.1763","article-title":"Close contacts with the endoplasmic reticulum as determinants of mitochondrial Ca2+ responses","volume":"280","author":"Rizzuto","year":"1998","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib76","doi-asserted-by":"crossref","first-page":"96","DOI":"10.1093\/emboj\/18.1.96","article-title":"Quasi-synaptic calcium signal transmission between endoplasmic reticulum and mitochondria","volume":"18","author":"Csordas","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.phrs.2026.108428_bib77","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.molcel.2010.04.003","article-title":"Ca2+ hot spots on the mitochondrial surface are generated by Ca2+ mobilization from stores, but not by activation of store-operated Ca2+ channels","volume":"38","author":"Giacomello","year":"2010","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib78","doi-asserted-by":"crossref","first-page":"6779","DOI":"10.1038\/s41467-022-34365-8","article-title":"Capture at the ER-mitochondrial contacts licenses IP(3) receptors to stimulate local Ca(2+) transfer and oxidative metabolism","volume":"13","author":"Katona","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib79","article-title":"Supralinear Dependence of the IP(3) Receptor-to-Mitochondria Local Ca(2+) Transfer on the Endoplasmic Reticulum Ca(2+) Loading","volume":"7","author":"Csordas","year":"2024","journal-title":"Contact (Thousand Oaks)"},{"key":"10.1016\/j.phrs.2026.108428_bib80","doi-asserted-by":"crossref","first-page":"42273","DOI":"10.1074\/jbc.M305248200","article-title":"Plasticity of mitochondrial calcium signaling","volume":"278","author":"Csordas","year":"2003","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib81","doi-asserted-by":"crossref","first-page":"17081","DOI":"10.1074\/jbc.RA118.002332","article-title":"Slow activation of fast mitochondrial Ca(2+) uptake by cytosolic Ca(2)","volume":"293","author":"Basso","year":"2018","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib82","doi-asserted-by":"crossref","first-page":"566","DOI":"10.1038\/nrm3412","article-title":"Mitochondria as sensors and regulators of calcium signalling","volume":"13","author":"Rizzuto","year":"2012","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib83","doi-asserted-by":"crossref","first-page":"1426","DOI":"10.1111\/j.1471-4159.2007.04825.x","article-title":"IP3 receptor\/Ca2+ channel: from discovery to new signaling concepts","volume":"102","author":"Mikoshiba","year":"2007","journal-title":"J. Neurochem."},{"key":"10.1016\/j.phrs.2026.108428_bib84","doi-asserted-by":"crossref","DOI":"10.1016\/j.ceca.2023.102770","article-title":"Understanding IP(3)R channels: From structural underpinnings to ligand-dependent conformational landscape","volume":"114","author":"Baker","year":"2023","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib85","doi-asserted-by":"crossref","first-page":"1408","DOI":"10.1038\/s41467-022-29073-2","article-title":"Structural basis for activation and gating of IP(3) receptors","volume":"13","author":"Schmitz","year":"2022","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib86","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1016\/j.ceca.2019.02.006","article-title":"Redox regulation of ER and mitochondrial Ca(2+) signaling in cell survival and death","volume":"79","author":"Joseph","year":"2019","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib87","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.2216857120","article-title":"Redox states in the endoplasmic reticulum directly regulate the activity of calcium channel, inositol 1,4,5-trisphosphate receptors","volume":"120","author":"Fujii","year":"2023","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2026.108428_bib88","doi-asserted-by":"crossref","first-page":"415","DOI":"10.1016\/0092-8674(95)90430-1","article-title":"Decoding of cytosolic calcium oscillations in the mitochondria","volume":"82","author":"Hajnoczky","year":"1995","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib89","doi-asserted-by":"crossref","first-page":"1261","DOI":"10.1152\/physrev.00006.2016","article-title":"The Inositol Trisphosphate\/Calcium Signaling Pathway in Health and Disease","volume":"96","author":"Berridge","year":"2016","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.phrs.2026.108428_bib90","doi-asserted-by":"crossref","first-page":"8170","DOI":"10.1074\/jbc.M113.504159","article-title":"Isoform- and species-specific control of inositol 1,4,5-trisphosphate (IP3) receptors by reactive oxygen species","volume":"289","author":"Bansaghi","year":"2014","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib91","doi-asserted-by":"crossref","first-page":"1113","DOI":"10.1083\/jcb.201006121","article-title":"NADPH oxidase links endoplasmic reticulum stress, oxidative stress, and PKR activation to induce apoptosis","volume":"191","author":"Li","year":"2010","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib92","doi-asserted-by":"crossref","first-page":"3866","DOI":"10.1016\/j.molcel.2021.07.014","article-title":"Oxidative bursts of single mitochondria mediate retrograde signaling toward the ER","volume":"81","author":"Booth","year":"2021","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib93","doi-asserted-by":"crossref","DOI":"10.15252\/embj.2019103530","article-title":"Nox4 regulates InsP(3) receptor-dependent Ca(2+) release into mitochondria to promote cell survival","volume":"39","author":"Beretta","year":"2020","journal-title":"EMBO J."},{"key":"10.1016\/j.phrs.2026.108428_bib94","first-page":"13349","article-title":"Hypoxic modulation of Ca2+ signaling in human venous endothelial cells","volume":"280","author":"Aley","year":"2005","journal-title":"Mult. roles React. Oxyg. Species J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib95","doi-asserted-by":"crossref","first-page":"196","DOI":"10.1016\/j.cmet.2011.05.014","article-title":"Ryanodine receptor oxidation causes intracellular calcium leak and muscle weakness in aging","volume":"14","author":"Andersson","year":"2011","journal-title":"Cell. Metab."},{"key":"10.1016\/j.phrs.2026.108428_bib96","doi-asserted-by":"crossref","first-page":"318","DOI":"10.1016\/S0891-5849(97)00227-X","article-title":"Glutathione is a cofactor for H2O2-mediated stimulation of Ca2+-induced Ca2+ release in cardiac myocytes","volume":"24","author":"Suzuki","year":"1998","journal-title":"Free. Radic. Biol. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib97","doi-asserted-by":"crossref","first-page":"539","DOI":"10.4067\/S0716-97602004000400007","article-title":"Redox regulation of RyR-mediated Ca2+ release in muscle and neurons","volume":"37","author":"Hidalgo","year":"2004","journal-title":"Biol. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib98","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1016\/j.ceca.2006.08.016","article-title":"Mitochondrial calcium signalling and cell death: approaches for assessing the role of mitochondrial Ca2+ uptake in apoptosis","volume":"40","author":"Hajnoczky","year":"2006","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib99","doi-asserted-by":"crossref","first-page":"6407","DOI":"10.1038\/onc.2008.308","article-title":"Calcium and apoptosis: ER-mitochondria Ca2+ transfer in the control of apoptosis","volume":"27","author":"Pinton","year":"2008","journal-title":"Oncogene"},{"key":"10.1016\/j.phrs.2026.108428_bib100","doi-asserted-by":"crossref","first-page":"349","DOI":"10.1054\/ceca.2000.0169","article-title":"Control of apoptosis by IP(3) and ryanodine receptor driven calcium signals","volume":"28","author":"Hajnoczky","year":"2000","journal-title":"Cell. Calcium"},{"key":"10.1016\/j.phrs.2026.108428_bib101","doi-asserted-by":"crossref","first-page":"1115","DOI":"10.1083\/jcb.200212059","article-title":"Caspase cleavage product of BAP31 induces mitochondrial fission through endoplasmic reticulum calcium signals, enhancing cytochrome c release to the cytosol","volume":"160","author":"Breckenridge","year":"2003","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib102","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1038\/emm.1999.9","article-title":"Redox signaling: hydrogen peroxide as intracellular messenger","volume":"31","author":"Rhee","year":"1999","journal-title":"Exp. Mol. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib103","doi-asserted-by":"crossref","first-page":"3553","DOI":"10.1128\/MCB.01445-09","article-title":"Nox4-derived H2O2 mediates endoplasmic reticulum signaling through local Ras activation","volume":"30","author":"Wu","year":"2010","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib104","doi-asserted-by":"crossref","first-page":"3554","DOI":"10.1038\/s41467-025-58909-w","article-title":"Lysosomal lipid peroxidation contributes to ferroptosis induction via lysosomal membrane permeabilization","volume":"16","author":"Saimoto","year":"2025","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib105","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2025.116486","article-title":"The ER thioredoxin-related transmembrane protein TMX2 controls redox-mediated tethering of ER-mitochondria contacts","volume":"44","author":"Chen","year":"2025","journal-title":"Cell. Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib106","doi-asserted-by":"crossref","first-page":"21288","DOI":"10.1073\/pnas.2003847117","article-title":"Selenoprotein N is an endoplasmic reticulum calcium sensor that links luminal calcium levels to a redox activity","volume":"117","author":"Chernorudskiy","year":"2020","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2026.108428_bib107","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1113\/jphysiol.2003.049478","article-title":"Mitochondrial formation of reactive oxygen species","volume":"552","author":"Turrens","year":"2003","journal-title":"J. Physiol."},{"key":"10.1016\/j.phrs.2026.108428_bib108","doi-asserted-by":"crossref","first-page":"221","DOI":"10.1016\/j.cell.2005.05.011","article-title":"Electron transfer between cytochrome c and p66Shc generates reactive oxygen species that trigger mitochondrial apoptosis","volume":"122","author":"Giorgio","year":"2005","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib109","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1089\/ars.2019.7929","article-title":"The Determining Role of Mitochondrial Reactive Oxygen Species Generation and Monoamine Oxidase Activity in Doxorubicin-Induced Cardiotoxicity","volume":"34","author":"Antonucci","year":"2021","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.phrs.2026.108428_bib110","doi-asserted-by":"crossref","DOI":"10.1016\/j.redox.2022.102410","article-title":"Transfer of H(2)O(2) from Mitochondria to the endoplasmic reticulum via Aquaporin-11","volume":"55","author":"Sorrentino","year":"2022","journal-title":"Redox Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib111","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.jmb.2010.12.039","article-title":"Two endoplasmic reticulum PDI peroxidases increase the efficiency of the use of peroxide during disulfide bond formation","volume":"406","author":"Nguyen","year":"2011","journal-title":"J. Mol. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib112","doi-asserted-by":"crossref","first-page":"1666","DOI":"10.1089\/ars.2012.4966","article-title":"PRDX4, an endoplasmic reticulum-localized peroxiredoxin at the crossroads between enzymatic oxidative protein folding and nonenzymatic protein oxidation","volume":"18","author":"Zito","year":"2013","journal-title":"Antioxid. Redox Signal."},{"key":"10.1016\/j.phrs.2026.108428_bib113","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.freeradbiomed.2014.01.018","article-title":"GPx8 peroxidase prevents leakage of H2O2 from the endoplasmic reticulum","volume":"70","author":"Ramming","year":"2014","journal-title":"Free. Radic. Biol. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib114","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1083\/jcb.200307010","article-title":"Ca2+-dependent redox modulation of SERCA 2b by ERp57","volume":"164","author":"Li","year":"2004","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib115","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1038\/s41419-017-0033-4","article-title":"Redox crosstalk at endoplasmic reticulum (ER) membrane contact sites (MCS) uses toxic waste to deliver messages","volume":"9","author":"Yoboue","year":"2018","journal-title":"Cell. Death Dis."},{"key":"10.1016\/j.phrs.2026.108428_bib116","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1083\/jcb.200105057","article-title":"VDAC-dependent permeabilization of the outer mitochondrial membrane by superoxide induces rapid and massive cytochrome c release","volume":"155","author":"Madesh","year":"2001","journal-title":"J. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib117","doi-asserted-by":"crossref","first-page":"250","DOI":"10.1007\/s00018-024-05286-0","article-title":"Redox regulation of UPR signalling and mitochondrial ER contact sites","volume":"81","author":"Casas-Martinez","year":"2024","journal-title":"Cell. Mol. Life Sci."},{"key":"10.1016\/j.phrs.2026.108428_bib118","doi-asserted-by":"crossref","first-page":"1559","DOI":"10.1073\/pnas.0908540107","article-title":"Leaky RyR2 trigger ventricular arrhythmias in Duchenne muscular dystrophy","volume":"107","author":"Fauconnier","year":"2010","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.phrs.2026.108428_bib119","article-title":"Interactions between sarco-endoplasmic reticulum and mitochondria in cardiac and skeletal muscle - pivotal roles in Ca(2)(+) and reactive oxygen species signaling","author":"Eisner","year":"2013","journal-title":"J. Cell. Sci. 126 2965-2978"},{"key":"10.1016\/j.phrs.2026.108428_bib120","doi-asserted-by":"crossref","first-page":"621","DOI":"10.1038\/nrm2952","article-title":"Mitochondria and cell death: outer membrane permeabilization and beyond","volume":"11","author":"Tait","year":"2010","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib121","doi-asserted-by":"crossref","first-page":"1111","DOI":"10.1152\/physrev.00001.2015","article-title":"The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology","volume":"95","author":"Bernardi","year":"2015","journal-title":"Physiol. Rev."},{"key":"10.1016\/j.phrs.2026.108428_bib122","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1126\/science.1081208","article-title":"BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis","volume":"300","author":"Scorrano","year":"2003","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib123","doi-asserted-by":"crossref","first-page":"982","DOI":"10.1101\/gad.12.7.982","article-title":"CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum","volume":"12","author":"Zinszner","year":"1998","journal-title":"Genes. Dev."},{"key":"10.1016\/j.phrs.2026.108428_bib124","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.1016\/j.cell.2007.04.027","article-title":"ER stress triggers apoptosis by activating BH3-only protein Bim","volume":"129","author":"Puthalakath","year":"2007","journal-title":"Cell"},{"key":"10.1016\/j.phrs.2026.108428_bib125","doi-asserted-by":"crossref","first-page":"1249","DOI":"10.1128\/MCB.21.4.1249-1259.2001","article-title":"Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state","volume":"21","author":"McCullough","year":"2001","journal-title":"Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib126","doi-asserted-by":"crossref","first-page":"157","DOI":"10.1002\/9780470725207.ch11","article-title":"The mitochondrial permeability transition pore","volume":"287","author":"Bernardi","year":"2007","journal-title":"Novartis Found. Symp."},{"key":"10.1016\/j.phrs.2026.108428_bib127","doi-asserted-by":"crossref","first-page":"975","DOI":"10.1083\/jcb.142.4.975","article-title":"Transient mitochondrial depolarizations reflect focal sarcoplasmic reticular calcium release in single rat cardiomyocytes","volume":"142","author":"Duchen","year":"1998","journal-title":"J. Cell. Biol."},{"issue":"Pt 2","key":"10.1016\/j.phrs.2026.108428_bib128","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1042\/bj3430311","article-title":"Fluctuations in mitochondrial membrane potential caused by repetitive gating of the permeability transition pore","volume":"343","author":"Huser","year":"1999","journal-title":"Biochem. J."},{"key":"10.1016\/j.phrs.2026.108428_bib129","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1007\/164_2016_129","article-title":"Mitochondrial Flashes: Elemental Signaling Events in Eukaryotic Cells","volume":"240","author":"Feng","year":"2017","journal-title":"Handb. Exp. Pharmacol."},{"key":"10.1016\/j.phrs.2026.108428_bib130","doi-asserted-by":"crossref","first-page":"6349","DOI":"10.1093\/emboj\/18.22.6349","article-title":"Apoptosis driven by IP(3)-linked mitochondrial calcium signals","volume":"18","author":"Szalai","year":"1999","journal-title":"EMBO J."},{"key":"10.1016\/j.phrs.2026.108428_bib131","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.yjmcc.2014.08.018","article-title":"The mitochondrial permeability transition: a current perspective on its identity and role in ischaemia\/reperfusion injury","volume":"78","author":"Halestrap","year":"2015","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.phrs.2026.108428_bib132","doi-asserted-by":"crossref","first-page":"355","DOI":"10.3389\/fphys.2014.00355","article-title":"Bcl-xL in neuroprotection and plasticity","volume":"5","author":"Jonas","year":"2014","journal-title":"Front. Physiol."},{"key":"10.1016\/j.phrs.2026.108428_bib133","doi-asserted-by":"crossref","first-page":"1800","DOI":"10.1161\/CIRCRESAHA.116.305421","article-title":"Regulated necrotic cell death: the passive aggressive side of Bax and Bak","volume":"116","author":"Karch","year":"2015","journal-title":"Circ. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib134","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1016\/j.molcel.2016.02.019","article-title":"Mitochondria-Judges and Executioners of Cell Death Sentences","volume":"61","author":"Bhola","year":"2016","journal-title":"Mol. Cell."},{"key":"10.1016\/j.phrs.2026.108428_bib135","doi-asserted-by":"crossref","first-page":"24","DOI":"10.1186\/s12915-017-0367-5","article-title":"TriPer, an optical probe tuned to the endoplasmic reticulum tracks changes in luminal H(2)O(2)","volume":"15","author":"Melo","year":"2017","journal-title":"BMC Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib136","doi-asserted-by":"crossref","first-page":"1287","DOI":"10.1038\/s41467-019-09253-3","article-title":"Coming together to define membrane contact sites","volume":"10","author":"Scorrano","year":"2019","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib137","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1038\/s41580-025-00864-x","article-title":"Key challenges and recommendations for defining organelle membrane contact sites","volume":"26","author":"Cali","year":"2025","journal-title":"Nat. Rev. Mol. Cell. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib138","doi-asserted-by":"crossref","first-page":"e171","DOI":"10.1161\/CIRCRESAHA.122.321833","article-title":"Enhanced Mitochondria-SR Tethering Triggers Adaptive Cardiac Muscle Remodeling","volume":"132","author":"Nichtova","year":"2023","journal-title":"Circ. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib139","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1038\/s41589-025-01918-z","article-title":"Repurposing salicylic acid as a versatile inducer of proximity","volume":"21","author":"Wang","year":"2025","journal-title":"Nat. Chem. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib140","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/j.cbpa.2019.11.006","article-title":"Inhibitors of the mitochondrial calcium uniporter for the treatment of disease","volume":"55","author":"Woods","year":"2020","journal-title":"Curr. Opin. Chem. Biol."},{"key":"10.1016\/j.phrs.2026.108428_bib141","doi-asserted-by":"crossref","first-page":"135","DOI":"10.1016\/j.yjmcc.2020.09.014","article-title":"Pharmacological inhibition of the mitochondrial Ca(2+) uniporter: Relevance for pathophysiology and human therapy","volume":"151","author":"Marta","year":"2021","journal-title":"J. Mol. Cell. Cardiol."},{"key":"10.1016\/j.phrs.2026.108428_bib142","doi-asserted-by":"crossref","DOI":"10.1016\/j.celrep.2021.109275","article-title":"Identification and functional validation of FDA-approved positive and negative modulators of the mitochondrial calcium uniporter","volume":"35","author":"De Mario","year":"2021","journal-title":"Cell. Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib143","doi-asserted-by":"crossref","first-page":"2321","DOI":"10.1016\/j.celrep.2020.01.081","article-title":"A High-Throughput Screening Identifies MICU1 Targeting Compounds","volume":"30","author":"Di Marco","year":"2020","journal-title":"Cell. Rep."},{"key":"10.1016\/j.phrs.2026.108428_bib144","doi-asserted-by":"crossref","DOI":"10.1016\/j.xcrm.2024.101439","article-title":"SEPN1-related myopathy depends on the oxidoreductase ERO1A and is druggable with the chemical chaperone TUDCA","author":"Germani","year":"2024","journal-title":"Cell. Rep. Med."},{"key":"10.1016\/j.phrs.2026.108428_bib145","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1038\/s41419-025-07426-1","article-title":"Small molecule-mediated inhibition of the oxidoreductase ERO1A restrains aggressive breast cancer by impairing VEGF and PD-L1 in the tumor microenvironment","volume":"16","author":"Varone","year":"2025","journal-title":"Cell. Death Dis."},{"key":"10.1016\/j.phrs.2026.108428_bib146","doi-asserted-by":"crossref","DOI":"10.1016\/j.phrs.2025.108037","article-title":"Pyrazolone-based ERO1 inhibitors in ERO1-driven triple-negative breast cancer and SEPN1-related myopathy: structure-activity relationship and therapeutic potential","author":"Retini","year":"2025","journal-title":"Pharmacol. Res."},{"key":"10.1016\/j.phrs.2026.108428_bib147","article-title":"Fingerprint of the oxido-reductase ERO1: a protein disulfide bond producer and supporter of cancer","volume":"1879","author":"Zito","year":"2023","journal-title":"Biochim. Biophys. Acta Rev. Cancer"},{"key":"10.1016\/j.phrs.2026.108428_bib148","doi-asserted-by":"crossref","first-page":"20993","DOI":"10.1074\/jbc.M110.126599","article-title":"A small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity","volume":"285","author":"Blais","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1016\/j.phrs.2026.108428_bib149","article-title":"A chemical chaperone improves muscle function in mice with a RyR1 mutation","volume":"8","author":"Lee","year":"2017","journal-title":"Nat. Commun."},{"key":"10.1016\/j.phrs.2026.108428_bib150","doi-asserted-by":"crossref","first-page":"1137","DOI":"10.1126\/science.1128294","article-title":"Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes","volume":"313","author":"Ozcan","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.phrs.2026.108428_bib151","doi-asserted-by":"crossref","DOI":"10.15252\/embj.201899576","article-title":"Lipin1 deficiency causes sarcoplasmic reticulum stress and chaperone-responsive myopathy","volume":"38","author":"Rashid","year":"2019","journal-title":"EMBO J."}],"container-title":["Pharmacological Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661826003439?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1043661826003439?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T10:50:07Z","timestamp":1789901407000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1043661826003439"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2026,10]]},"references-count":151,"alternative-id":["S1043661826003439"],"URL":"https:\/\/doi.org\/10.1016\/j.phrs.2026.108428","relation":{},"ISSN":["1043-6618"],"issn-type":[{"value":"1043-6618","type":"print"}],"subject":[],"published":{"date-parts":[[2026,10]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Crosstalk between UPR and mitochondria: The triad of ER\u2013mitochondria contacts, Ca\u00b2\u207a, and ROS","name":"articletitle","label":"Article Title"},{"value":"Pharmacological Research","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.phrs.2026.108428","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2026 The Authors. Published by Elsevier Ltd.","name":"copyright","label":"Copyright"}],"article-number":"108428"}}